1im2
From Proteopedia
(New page: 200px<br /><applet load="1im2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1im2, resolution 2.80Å" /> '''HslU, Haemophilus In...) |
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| - | [[Image:1im2.jpg|left|200px]]<br /><applet load="1im2" size=" | + | [[Image:1im2.jpg|left|200px]]<br /><applet load="1im2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1im2, resolution 2.80Å" /> | caption="1im2, resolution 2.80Å" /> | ||
'''HslU, Haemophilus Influenzae, Selenomethionine Variant'''<br /> | '''HslU, Haemophilus Influenzae, Selenomethionine Variant'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the Haemophilus influenzae HslU protein, a molecular | + | The structure of the Haemophilus influenzae HslU protein, a molecular chaperone of the Clp/Hsp100 family, has been solved to 2.3 A by molecular replacement using a model of the homologous Escherichia coli protein. The crystals in which the structure was solved have an unusual twinning, or one-dimensional disorder, in which each successive crystal-packing layer is displaced laterally relative to the one below it. A model for the twinning and an algorithm for detwinning the data are described. It is known from other work that when the HslU hexamer binds its cognate protease HslV, the carboxy-terminal helices of HslU protomers distend and bind between HslV subunits. Comparison of HslU alone with its structure in the HslUV complex reveals several conserved amino-acid residues whose side-chain interactions differ between the two structures, suggesting that they may be part of a conformational switch that facilitates the release of the HslU carboxy-terminal helices when HslV binds. |
==About this Structure== | ==About this Structure== | ||
| - | 1IM2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with SO4 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1IM2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IM2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: McKay, D | + | [[Category: McKay, D B.]] |
| - | [[Category: Trame, C | + | [[Category: Trame, C B.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: chaperone]] | [[Category: chaperone]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:13 2008'' |
Revision as of 11:13, 21 February 2008
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HslU, Haemophilus Influenzae, Selenomethionine Variant
Overview
The structure of the Haemophilus influenzae HslU protein, a molecular chaperone of the Clp/Hsp100 family, has been solved to 2.3 A by molecular replacement using a model of the homologous Escherichia coli protein. The crystals in which the structure was solved have an unusual twinning, or one-dimensional disorder, in which each successive crystal-packing layer is displaced laterally relative to the one below it. A model for the twinning and an algorithm for detwinning the data are described. It is known from other work that when the HslU hexamer binds its cognate protease HslV, the carboxy-terminal helices of HslU protomers distend and bind between HslV subunits. Comparison of HslU alone with its structure in the HslUV complex reveals several conserved amino-acid residues whose side-chain interactions differ between the two structures, suggesting that they may be part of a conformational switch that facilitates the release of the HslU carboxy-terminal helices when HslV binds.
About this Structure
1IM2 is a Single protein structure of sequence from Haemophilus influenzae with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of Haemophilus influenzae HslU protein in crystals with one-dimensional disorder twinning., Trame CB, McKay DB, Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1079-90. Epub 2001, Jul 23. PMID:11468391
Page seeded by OCA on Thu Feb 21 13:13:13 2008
